ID B4DDD6_HUMAN Unreviewed; 406 AA. AC B4DDD6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 117. DE SubName: Full=Drebrin like {ECO:0000313|Ensembl:ENSP00000405343.1}; DE SubName: Full=cDNA FLJ59450, highly similar to Drebrin-like protein {ECO:0000313|EMBL:BAG56697.1}; GN Name=DBNL {ECO:0000313|Ensembl:ENSP00000405343.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG56697.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000405343.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] {ECO:0007829|PubMed:15144186} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [3] {ECO:0007829|PubMed:15592455} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [4] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] {ECO:0007829|PubMed:16964243} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [6] {ECO:0000313|EMBL:BAG56697.1} RP NUCLEOTIDE SEQUENCE. RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0007829|PubMed:18088087} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schutz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [8] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] {ECO:0000313|Ensembl:ENSP00000405343.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection, CC dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, CC lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell projection, neuron CC projection {ECO:0000256|ARBA:ARBA00004487}. Cell projection, podosome CC {ECO:0000256|ARBA:ARBA00004188}. Cell projection, ruffle CC {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cell cortex CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle, clathrin-coated CC vesicle membrane {ECO:0000256|ARBA:ARBA00004145}; Peripheral membrane CC protein {ECO:0000256|ARBA:ARBA00004145}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004145}. Early endosome CC {ECO:0000256|ARBA:ARBA00004412}. Endosome CC {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004255}. Perikaryon CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density CC {ECO:0000256|ARBA:ARBA00034105}. Synapse CC {ECO:0000256|ARBA:ARBA00034103}. CC -!- SIMILARITY: Belongs to the ABP1 family. CC {ECO:0000256|ARBA:ARBA00011039}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC017116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK293151; BAG56697.1; -; mRNA. DR ProteomicsDB; 3849; -. DR Antibodypedia; 13203; 295 antibodies from 35 providers. DR Ensembl; ENST00000452943.5; ENSP00000405343.1; ENSG00000136279.21. DR UCSC; uc011kbm.3; human. DR HGNC; HGNC:2696; DBNL. DR VEuPathDB; HostDB:ENSG00000136279; -. DR GeneTree; ENSGT00940000156732; -. DR HOGENOM; CLU_013085_0_0_1; -. DR ChiTaRS; DBNL; human. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000136279; Expressed in lower esophagus mucosa and 164 other cell types or tissues. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR CDD; cd11281; ADF_drebrin_like; 1. DR CDD; cd11960; SH3_Abp1_eu; 1. DR Gene3D; 3.40.20.10; Severin; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR035717; Drebrin-like_SH3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1. DR PANTHER; PTHR10829:SF12; DREBRIN-LIKE PROTEIN; 1. DR Pfam; PF00241; Cofilin_ADF; 1. DR Pfam; PF14604; SH3_9; 1. DR SMART; SM00102; ADF; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51263; ADF_H; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Actin-binding {ECO:0000256|ARBA:ARBA00023203}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Membrane {ECO:0000256|ARBA:ARBA00022475}; KW Proteomics identification {ECO:0007829|EPD:B4DDD6, KW ECO:0007829|MaxQB:B4DDD6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}. FT DOMAIN 4..137 FT /note="ADF-H" FT /evidence="ECO:0000259|PROSITE:PS51263" FT DOMAIN 347..406 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 183..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 273..298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 183..201 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..241 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..259 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 406 AA; 45746 MW; 702D5CEB34EC2350 CRC64; MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG KVMYAFCRVK DPNSGLPKFV LINWGAHVTI NARAEEDVEP ECIMEKVAKA SGANYSFHKE SGRFQDVGPQ APVGSVYQKT NAVSEIKRVG KDSFWAKAEK EEENRRLEEK RRAEEAQRQL EQERRERELR EAARREQRYQ EQGGEASPQS RTWEQQQEVV SRNRNEQESA VHPREIFKQK ERAMSTTSIS SPQPGKLRSP FLQKQLTQPE THFGREPAAA ISRPRADLPA EEPAPSTPPC LVQAEEEAVY EEPPEQETFY EQPPLVQQQG AGSEHIDHHI QGQGLSGQGL CARALYDYQA ADDTEISFDP ENLITGIEVI DEGWWRGYGP DGHFGMFPAN YVELIE //